3TDZ
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-stapled acetylated Ubc12N complex
Summary for 3TDZ
Entry DOI | 10.2210/pdb3tdz/pdb |
Related | 3TDI 3TDU |
Related PRD ID | PRD_001077 |
Descriptor | DCN1-like protein 1, Cullin-1, STAPLED PEPTIDE, ... (4 entities in total) |
Functional Keywords | e2:e3, protein binding-inhibitor complex, protein binding/inhibitor |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus : Q96GG9 |
Total number of polymer chains | 6 |
Total formula weight | 67602.14 |
Authors | Scott, D.C.,Monda, J.K.,Bennett, E.J.,Harper, J.W.,Schulman, B.A. (deposition date: 2011-08-11, release date: 2011-10-12, Last modification date: 2023-12-06) |
Primary citation | Scott, D.C.,Monda, J.K.,Bennett, E.J.,Harper, J.W.,Schulman, B.A. N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science, 334:674-678, 2011 Cited by PubMed: 21940857DOI: 10.1126/science.1209307 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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